Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1

Kent K. Arrell; Irina Neverova; Heather Fraser; Eduardo Marbán; Jennifer E. Van Eyk

doi:10.1161/hh1801.097240

Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1

Kent K. Arrell, Irina Neverova, Heather Fraser, Eduardo Marbán, Jennifer E. Van Eyk

Research output: Contribution to journal › Article › peer-review

90 Scopus citations

Abstract

Proteomic analysis of rabbit ventricular myocytes revealed a novel posttranslational modification to myosin light chain 1 (MLC1), consisting of phosphorylation at two sites. Subproteomic extraction to isolate myofilament-enriched fractions enabled determination of the extent of phosphorylation, which increased from 25.7±1.6% to 34.0±2.7% (mean±SE, n=4; P<0.05) after adenosine treatment at levels sufficient to pharmacologically precondition the myocytes (100μmol/L). Mass spectrometry of MLC1 tryptic digests identified two peptide fragments modified by phosphorylation. These two phosphopeptides were characterized by peptide mass fingerprinting to determine the phosphorylation sites within rabbit ventricular MLC1, which correspond to Thr69 and Ser200 of rat MLC1, and to Thr64 and Ser194 or 195 of human MLC1. This proteomic analysis of preconditioned myocardium has revealed a previously unsuspected in vivo posttranslational modification to MLC1.

Original language	English (US)
Pages (from-to)	480-487
Number of pages	8
Journal	Circulation research
Volume	89
Issue number	6
DOIs	https://doi.org/10.1161/hh1801.097240
State	Published - Sep 14 2001
Externally published	Yes

Keywords

Adenosine
Myosin light chain
Phosphorylation
Preconditioning
Proteomics

ASJC Scopus subject areas

Physiology
Cardiology and Cardiovascular Medicine

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10.1161/hh1801.097240

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title = "Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1",

abstract = "Proteomic analysis of rabbit ventricular myocytes revealed a novel posttranslational modification to myosin light chain 1 (MLC1), consisting of phosphorylation at two sites. Subproteomic extraction to isolate myofilament-enriched fractions enabled determination of the extent of phosphorylation, which increased from 25.7±1.6% to 34.0±2.7% (mean±SE, n=4; P<0.05) after adenosine treatment at levels sufficient to pharmacologically precondition the myocytes (100μmol/L). Mass spectrometry of MLC1 tryptic digests identified two peptide fragments modified by phosphorylation. These two phosphopeptides were characterized by peptide mass fingerprinting to determine the phosphorylation sites within rabbit ventricular MLC1, which correspond to Thr69 and Ser200 of rat MLC1, and to Thr64 and Ser194 or 195 of human MLC1. This proteomic analysis of preconditioned myocardium has revealed a previously unsuspected in vivo posttranslational modification to MLC1.",

keywords = "Adenosine, Myosin light chain, Phosphorylation, Preconditioning, Proteomics",

author = "Arrell, {Kent K.} and Irina Neverova and Heather Fraser and Eduardo Marb{\'a}n and {Van Eyk}, {Jennifer E.}",

year = "2001",

month = sep,

day = "14",

doi = "10.1161/hh1801.097240",

language = "English (US)",

volume = "89",

pages = "480--487",

journal = "Circulation research",

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T1 - Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1

AU - Arrell, Kent K.

AU - Neverova, Irina

AU - Fraser, Heather

AU - Marbán, Eduardo

AU - Van Eyk, Jennifer E.

PY - 2001/9/14

Y1 - 2001/9/14

N2 - Proteomic analysis of rabbit ventricular myocytes revealed a novel posttranslational modification to myosin light chain 1 (MLC1), consisting of phosphorylation at two sites. Subproteomic extraction to isolate myofilament-enriched fractions enabled determination of the extent of phosphorylation, which increased from 25.7±1.6% to 34.0±2.7% (mean±SE, n=4; P<0.05) after adenosine treatment at levels sufficient to pharmacologically precondition the myocytes (100μmol/L). Mass spectrometry of MLC1 tryptic digests identified two peptide fragments modified by phosphorylation. These two phosphopeptides were characterized by peptide mass fingerprinting to determine the phosphorylation sites within rabbit ventricular MLC1, which correspond to Thr69 and Ser200 of rat MLC1, and to Thr64 and Ser194 or 195 of human MLC1. This proteomic analysis of preconditioned myocardium has revealed a previously unsuspected in vivo posttranslational modification to MLC1.

AB - Proteomic analysis of rabbit ventricular myocytes revealed a novel posttranslational modification to myosin light chain 1 (MLC1), consisting of phosphorylation at two sites. Subproteomic extraction to isolate myofilament-enriched fractions enabled determination of the extent of phosphorylation, which increased from 25.7±1.6% to 34.0±2.7% (mean±SE, n=4; P<0.05) after adenosine treatment at levels sufficient to pharmacologically precondition the myocytes (100μmol/L). Mass spectrometry of MLC1 tryptic digests identified two peptide fragments modified by phosphorylation. These two phosphopeptides were characterized by peptide mass fingerprinting to determine the phosphorylation sites within rabbit ventricular MLC1, which correspond to Thr69 and Ser200 of rat MLC1, and to Thr64 and Ser194 or 195 of human MLC1. This proteomic analysis of preconditioned myocardium has revealed a previously unsuspected in vivo posttranslational modification to MLC1.

KW - Adenosine

KW - Myosin light chain

KW - Phosphorylation

KW - Preconditioning

KW - Proteomics

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JO - Circulation research

JF - Circulation research

IS - 6

ER -

Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1

Abstract

Keywords

ASJC Scopus subject areas

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